Rev is a key regulatory protein of HV-1. Its function is to bind to viral transcripts and effect export from the nucleus of unspliced mRNA thereby allowing the production of structural proteins. Despite its importance, the structure has only been recently determined due to the tendency of the protein to aggregate. Antibody antigen binding domains (Fab and scFv) can mediate co-crystallization of refractory proteins. Protein antibody complexes were produced which generated crystals from which the structure of Rev was determined by X-ray crystallography. The more recent higher resolution structure of Rev is being used to model the protein-protein interactions or self-associations which are essential for Rev action. Also, the functional interactions of Rev with RNA and accessory proteins are being studied with the aim of gathering structural information which may be useful for targeted anti-HIV intervention. HIV protease, a homodimeric protein is essential in the viral life cycle and a major anti-HIV drug target. Peptides derived from the N- and C-terminal regions of the HIV-1 protease dimer interface inhibit protease activity by preventing dimerization (monomeric protein is inactive). In previous work, it was shown that the solubility and cell permeability of the peptides was enhanced by linking the transduction domain of HIV-Tat. A genetic construct was generated that can be used to study the first step in the cascade of HIV-1 protease Gag-Pro-Pol processing and show that reversible oxidation of cysteines can control the activity of the HIV-1 protease at this initial step. This assay system also has the potential for the screening of potential dimerization inhibitors.